The deletion of six amino acids at the C-terminus of the alpha 1 (II) chain causes overmodification of type II and type XI collagen: further evidence for the association between small deletions in COL2A1 and Kniest dysplasia.

Details

Serval ID
serval:BIB_1737CD25F40A
Type
Article: article from journal or magazin.
Publication sub-type
Case report (case report): feedback on an observation with a short commentary.
Collection
Publications
Title
The deletion of six amino acids at the C-terminus of the alpha 1 (II) chain causes overmodification of type II and type XI collagen: further evidence for the association between small deletions in COL2A1 and Kniest dysplasia.
Journal
Journal of Medical Genetics
Author(s)
Winterpacht A., Superti-Furga A., Schwarze U., Stöss H., Steinmann B., Spranger J., Zabel B.
ISSN
0022-2593 (Print)
ISSN-L
0022-2593
Publication state
Published
Issued date
1996
Volume
33
Number
8
Pages
649-654
Language
english
Notes
Publication types: Case Reports ; Journal Article ; Research Support, Non-U.S. Gov't
Abstract
We have identified an 18 bp deletion in exon 49 of the type II procollagen gene (COL2A1) in a patient with Kniest dysplasia. The deletion is located at the very C-terminus of the helical domain and removes two of three Gly-Pro-Pro triplets at positions 1007-1012, which are thought to be involved in helix formation and stability. Morphological investigation of an iliac crest biopsy showed large inclusions in the endoplasmic reticulum of chondrocytes, reflecting impaired secretion of type II collagen. Electrophoretic analysis of collagens extracted from cartilage or synthesised by cultured chondrocytes showed that type II and also type XI procollagen molecules containing mutant alpha 1 (II) chains showed post-translational overmodification. These observations provide further evidence for the general association of Kniest dysplasia with small deletions in the helical domain of type II collagen.
Keywords
Amino Acid Sequence, Base Sequence, Cartilage/chemistry, Cartilage/cytology, Cells, Cultured, Child, Preschool, Collagen/biosynthesis, DNA Mutational Analysis, Endoplasmic Reticulum, Rough/ultrastructure, Exons/genetics, Genes/genetics, Humans, Ilium, Inclusion Bodies, Male, Molecular Sequence Data, Osteochondrodysplasias/genetics, Osteochondrodysplasias/metabolism, Procollagen/genetics, Sequence Deletion/genetics
Pubmed
Web of science
Create date
14/03/2011 17:14
Last modification date
20/08/2019 13:47
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